 |
PDBsum entry 2x72
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Signaling protein
|
PDB id
|
|
|
|
2x72
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The structural basis of agonist-Induced activation in constitutively active rhodopsin.
|
|
|
Authors
|
|
J.Standfuss,
P.C.Edwards,
A.D'Antona,
M.Fransen,
G.Xie,
D.D.Oprian,
G.F.Schertler.
|
|
|
Ref.
|
|
Nature, 2011,
471,
656-660.
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
No abstract given.
|
|
|
Secondary reference #1
|
|
|
Title
|
|
Crystal structure of a thermally stable rhodopsin mutant.
|
|
|
Authors
|
|
J.Standfuss,
G.Xie,
P.C.Edwards,
M.Burghammer,
D.D.Oprian,
G.F.Schertler.
|
|
|
Ref.
|
|
J Mol Biol, 2007,
372,
1179-1188.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Figure 4.
Figure 4. Electron density maps of N2C/D282C rhodopsin. (a)
Retinal omit electron density map (0.75 σ) obtained after
molecular replacement and density modification. The retinal
(red) was not included but appears clearly in the electron
density. (b) Disulfide bond and N15 glycosylation. The
σA-weighted 2F[o] – F[c] with electron density contoured at
0.9σ. The disulfide bond between the mutated residues C2 and
C282 is well resolved, as is the first residue of the
N-glycosylation linked to N15. No density is visible adjacent to
the mutated residue 2, which would have been glycosylated in
wild-type rhodopsin.
|
|
Figure 6.
Figure 6. The N-terminal cap domain. Contacts between the
N-terminal cap (blue) and the rest of the receptor (cyan). Atoms
of the receptor with a minimum distance of 5 Å to residues
1–33 of the N terminus are colored beige. The covalently bound
retinal (red) is separated from the N-terminal cap by the lid
formed from the E2 loop. The designed disulfide between C2 and
C282 connecting the N-terminal cap with loop E3 is shown as
yellow sticks. The molecule is viewed with the extracellular
site facing up.
|
|
|
|
|
|
The above figures are
reproduced from the cited reference
which is an Open Access publication published by Elsevier
|
|
|
|
|
|
|
